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P94248

- BGLFU_BIFBR

UniProt

P94248 - BGLFU_BIFBR

Protein

Bifunctional beta-D-glucosidase/beta-D-fucosidase

Gene
N/A
Organism
Bifidobacterium breve
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Bifunctional beta-D-glucosidase/beta-D-fucosidase. Activity towards pNP-beta-D-fucoside is about 80-85% of the activity towards pNP-beta-D-glucoside. Also has slight activity (less than 10%) towards pNP-beta-D-galactoside, and very low activity (less than 1%) towards pNP-beta-D-xyloside. Hydrolyzes laminaribiose, sophorose, cellobiose and gentobiose. Not active against maltose, pNP-alpha-D-glucoside or pNP-beta-L-fucoside.2 Publications

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.2 Publications
    Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides.2 Publications

    Enzyme regulationi

    Inhibited by Cu2+, Ag+ and Hg+, but not by other cations such as Mg2+, Ca2+, Mn2+ and Co2+. Inhibited by 1-amino-1-deoxy-D-glucose and p-chloromercuribenzoic acid, but not by EDTA or dithiothreitol. Inhibited by the disaccharides sucrose, lactose and cellobiose. The monosaccharides D-fructose, D-mannose, D-xylose and D-glucose increase the beta-D-fucosidase activity, but not the beta-D-glucosidase activity. D-glucose inhibits the beta-D-glucosidase activity, but promotes the beta-D-fucosidase activity. D-fucose inhibits the beta-D-glucosidase activity and does not significantly affect the beta-D-fucosidase activity.1 Publication

    Kineticsi

    1. KM=1.3 mM for pNP-beta-D-glucoside2 Publications
    2. KM=0.7 mM for pNP-beta-D-fucoside2 Publications

    pH dependencei

    Optimum pH is 5.5 with pNP-beta-D-glucoside as a substrate. Retains more than 90% of its activity between pH 5.0 and 7.0. Retains 70% of its activity at pH 4.5 and 8.5.2 Publications

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius with pNP-beta-D-glucoside as a substrate. Retains 60% of its activity after 10 minutes incubation at 50 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei168 – 1681Proton donorBy similarity
    Active sitei362 – 3621NucleophileBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. beta-D-fucosidase activity Source: UniProtKB-EC
    2. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional beta-D-glucosidase/beta-D-fucosidase (EC:3.2.1.21, EC:3.2.1.38)
    OrganismiBifidobacterium breve
    Taxonomic identifieri1685 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 460459Bifunctional beta-D-glucosidase/beta-D-fucosidase1 PublicationPRO_0000395428Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP94248.
    SMRiP94248. Positions 2-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Sequence Analysis

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR017736. Glyco_hydro_1_beta-glucosidase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR03356. BGL. 1 hit.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P94248-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTMIFPKGFM FGTATAAYQI EGAVAEGGRT PSIWDTFSHT GHTLNGDTGD    50
    VADDFYHRWE DDLKLLRDLG VNAYRFSIGI PRVIPTPDGK PNQEGLDFYS 100
    RIVDRLLEYG IAPIVTLYHW DLPQYMASGD GREGGWLERE TAYRIADYAG 150
    IVAKCLGDRV HTYTTLNEPW CSAHLSYGGT EHAPGLGAGP LAFRAAHHLN 200
    LAHGLMCEAV RAEAGAKPGL SVTLNLQICR GDADAVHRVD LIGNRVFLDP 250
    MLRGRYPDEL FSITKGICDW GFVCDGDLDL IHQPIDVLGL NYYSTNLVKM 300
    SDRPQFPQST EASTAPGASD VDWLPTAGPH TEMGWNIDPD ALYETLVRLN 350
    DNYPGMPLVV TENGMACPDK VEVGTDGVKM VHDNDRIDYL RRHLEAVYRA 400
    IEEGTDVRGY FAWSLMDNFE WAFGYSKRFG LTYVDYESQE RVKKDSFDWY 450
    RRFIADHSAR 460
    Length:460
    Mass (Da):51,514
    Last modified:May 1, 1997 - v1
    Checksum:i5FD80CB8AB6888A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88311 Genomic DNA. Translation: BAA19881.1.
    PIRiJC5137.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88311 Genomic DNA. Translation: BAA19881.1 .
    PIRi JC5137.

    3D structure databases

    ProteinModelPortali P94248.
    SMRi P94248. Positions 2-458.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR017736. Glyco_hydro_1_beta-glucosidase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    TIGRFAMsi TIGR03356. BGL. 1 hit.
    PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequence of the beta-D-glucosidase gene from Bifidobacterium breve clb, and expression of beta-D-glucosidase activity in Escherichia coli."
      Nunoura N., Ohdan K., Tanaka K., Tamaki H., Yano T., Inui M., Yukawa H., Yamamoto K., Kumagai H.
      Biosci. Biotechnol. Biochem. 60:2011-2018(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "Purification and characterization of beta-D-glucosidase (beta-D-fucosidase) from Bifidobacterium breve clb acclimated to cellobiose."
      Nunoura N., Ohdan K., Yano T., Yamamoto K., Kumagai H.
      Biosci. Biotechnol. Biochem. 60:188-193(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiBGLFU_BIFBR
    AccessioniPrimary (citable) accession number: P94248
    Secondary accession number(s): O08487
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3